GLPQ1_MYCTU
ID GLPQ1_MYCTU Reviewed; 274 AA.
AC P9WMU3; L0TGR7; P96236; Q7D4R6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Probable glycerophosphodiester phosphodiesterase 1;
DE Short=Glycerophosphoryl diester phosphodiesterase 1;
DE EC=3.1.4.46;
GN Name=glpQ1; OrderedLocusNames=Rv3842c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION BY HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes
CC deacylated phospholipids to G3P and the corresponding alcohols.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- INDUCTION: A possible member of the dormancy regulon. Induced in
CC response to reduced oxygen tension (hypoxia). It is hoped that this
CC regulon will give insight into the latent, or dormant phase of
CC infection. {ECO:0000269|PubMed:11416222}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46671.1; -; Genomic_DNA.
DR PIR; G70653; G70653.
DR RefSeq; NP_218359.1; NC_000962.3.
DR RefSeq; WP_003420924.1; NZ_NVQJ01000022.1.
DR AlphaFoldDB; P9WMU3; -.
DR SMR; P9WMU3; -.
DR STRING; 83332.Rv3842c; -.
DR PaxDb; P9WMU3; -.
DR DNASU; 886177; -.
DR GeneID; 45427843; -.
DR GeneID; 886177; -.
DR KEGG; mtu:Rv3842c; -.
DR TubercuList; Rv3842c; -.
DR eggNOG; COG0584; Bacteria.
DR OMA; ETKHPTR; -.
DR PhylomeDB; P9WMU3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 1: Evidence at protein level;
KW Calcium; Glycerol metabolism; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..274
FT /note="Probable glycerophosphodiester phosphodiesterase 1"
FT /id="PRO_0000392941"
FT DOMAIN 12..264
FT /note="GP-PDE"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 274 AA; 29917 MW; 8EBC81ED9BFDCBDF CRC64;
MTWADEVLAG HPFVVAHRGA SAARPEHTLA AYDLALKEGA DGVECDVRLT RDGHLVCVHD
RRLDRTSTGA GLVSTMTLAQ LRELEYGAWH DSWRPDGSHG DTSLLTLDAL VSLVLDWHRP
VKIFVETKHP VRYGSLVENK LLALLHRFGI AAPASADRSR AVVMSFSAAA VWRIRRAAPL
LPTVLLGKTP RYLTSSAATA VGATAVGPSL PALKEYPQLV DRSAAQGRAV YCWNVDEYED
IDFCREVGVA WIGTHHPGRT KAWLEDGRAN GTTR
